4l2m

Crystal structure of the 2/2 hemoglobin from Synechococcus sp. PCC 7002 in the cyanomet state and with covalently attached heme

spinqualitylabelsall models 4l2m, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4l2m is a 2 chain structure with sequence from Synechococcus sp. PCC 7002. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.25Å Ligands: CYN, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8RT58_PICP2 Publication Abstract from PubMed The X-ray structures of the hemoglobin from Synechococcus sp. PCC 7002 (GlbN) were solved in the ferric bis-histidine (1.44 A resolution) and cyanide-bound (2.25 A resolution) states with covalently attached heme. The two structures illustrate the conformational changes and cavity opening caused by exogenous ligand binding. They also reveal an unusually distorted heme, ruffled as in c cytochromes. Comparison to the solution structure demonstrates the influence of crystal packing on several structural elements, whereas comparison to GlbN from Synechocystis sp. PCC 6803 shows subtle differences in heme geometries and environment. The new structures will be instrumental in elucidating GlbN reactivity. (c) Proteins 2013;. (c) 2013 Wiley Periodicals, Inc. The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: Comparison of X-ray and NMR structures.,Wenke BB, Lecomte JT, Heroux A, Schlessman JL Proteins. 2013 Sep 2. doi: 10.1002/prot.24409. PMID:23999883 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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